Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers (Q34498607)

2 August 2017

Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers (English)

1 reference

2 August 2017

Christopher J. Schofield

9

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

Jürgen Brem

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

Opher Gileadi

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

Peter J McHugh

6

1 reference

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5 June 2020

Timothy R. Walsh

7

1 reference

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5 June 2020

author name string

Sander S van Berkel

2

1 reference

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5 June 2020

David Zollman

3

1 reference

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5 June 2020

Sook Y Lee

4

1 reference

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5 June 2020

Michael A McDonough

8

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5 June 2020

language of work or name

English

0 references

publication date

19 October 2015

1 reference

Antimicrobial Agents and Chemotherapy

2 August 2017

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

volume

60

1 reference

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5 June 2020

issue

1

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5 June 2020

page(s)

142-150

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Overcoming differences: The catalytic mechanism of metallo-β-lactamases

5 June 2020

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Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure de

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Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition

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Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

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Proliferation and significance of clinically relevant β-lactamases

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New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition

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Computational analysis of pathogen-borne metallo β-lactamases reveals discriminating structural features between B1 types

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Genetic and biochemical characterization of a novel metallo-β-lactamase, TMB-1, from an Achromobacter xylosoxidans strain isolated in Tripoli, Libya

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A structural view of the antibiotic degradation enzyme NDM-1 from a superbug

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The identification of new metallo-β-lactamase inhibitor leads from fragment-based screening.

7 July 2018

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Metallo-β-lactamases: a last frontier for β-lactams?

7 July 2018

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Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism

7 July 2018

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Biochemical and Structural Characterization of the Subclass B1 Metallo- -Lactamase VIM-4

7 July 2018

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Current challenges in antimicrobial chemotherapy: focus on ß-lactamase inhibition

7 July 2018

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Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India

7 July 2018

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Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols

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7 July 2018

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Identifiers

DOI

10.1128/AAC.01335-15

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:26482303%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

1 reference